View source for 6qj3


==Crystal structure of the C. thermophilum condensin Ycs4-Brn1 subcomplex==
<StructureSection load='6qj3' size='340' side='right'caption='[[6qj3]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qj3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum] and [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QJ3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6qj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qj3 OCA], [https://pdbe.org/6qj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qj3 RCSB], [https://www.ebi.ac.uk/pdbsum/6qj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qj3 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The condensin protein complex plays a key role in the structural organization of genomes. How the ATPase activity of its SMC subunits drives large-scale changes in chromosome topology has remained unknown. Here we reconstruct, at near-atomic resolution, the sequence of events that take place during the condensin ATPase cycle. We show that ATP binding induces a conformational switch in the Smc4 head domain that releases its hitherto undescribed interaction with the Ycs4 HEAT-repeat subunit and promotes its engagement with the Smc2 head into an asymmetric heterodimer. SMC head dimerization subsequently enables nucleotide binding at the second active site and disengages the Brn1 kleisin subunit from the Smc2 coiled coil to open the condensin ring. These large-scale transitions in the condensin architecture lay out a mechanistic path for its ability to extrude DNA helices into large loop structures.

Structural Basis of an Asymmetric Condensin ATPase Cycle.,Hassler M, Shaltiel IA, Kschonsak M, Simon B, Merkel F, Tharichen L, Bailey HJ, Macosek J, Bravo S, Metz J, Hennig J, Haering CH Mol Cell. 2019 Jun 20;74(6):1175-1188.e9. doi: 10.1016/j.molcel.2019.03.037. PMID:31226277<ref>PMID:31226277</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qj3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Condensin|Condensin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chaetomium thermophilum]]
[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
[[Category: Large Structures]]
[[Category: Haering CH]]
[[Category: Hassler M]]
[[Category: Kschonsak M]]